Protein structure comparison: implications for the nature of 'fold space', and structure and function prediction

Rachel Kolodny, Donald Petrey, Barry Honig

Research output: Contribution to journalArticlepeer-review

Abstract

The identification of geometric relationships between protein structures offers a powerful approach to predicting the structure and function of proteins. Methods to detect such relationships range from human pattern recognition to a variety of mathematical algorithms. A number of schemes for the classification of protein structure have found widespread use and these implicitly assume the organization of protein structure space into discrete categories. Recently, an alternative view has emerged in which protein fold space is seen as continuous and multidimensional. Significant relationships have been observed between proteins that belong to what have been termed different 'folds'. There has been progress in the use of these relationships in the prediction of protein structure and function.

Original languageEnglish
Pages (from-to)393-398
Number of pages6
JournalCurrent Opinion in Structural Biology
Volume16
Issue number3
DOIs
StatePublished - Jun 2006
Externally publishedYes

Bibliographical note

Funding Information:
We are grateful to Michael Levitt, Chris Tang, Mickey Kosloff and Burkhard Rost for many helpful discussions on the topics covered in this review. This work was supported in part by the Northeast Structural Genomics Consortium (NESG – GM074958). The thinking reflected in this review has evolved in part as a result of facing the challenges of NESG target selection.

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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